ID T1H9J5_RHOPR Unreviewed; 442 AA. AC T1H9J5; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 28-JUN-2023, entry version 49. DE RecName: Full=Semialdehyde dehydrogenase NAD-binding domain-containing protein {ECO:0000259|SMART:SM00859}; OS Rhodnius prolixus (Triatomid bug). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera; OC Cimicomorpha; Reduviidae; Triatominae; Rhodnius. OX NCBI_TaxID=13249 {ECO:0000313|EnsemblMetazoa:RPRC000698-PA, ECO:0000313|Proteomes:UP000015103}; RN [1] {ECO:0000313|Proteomes:UP000015103} RP NUCLEOTIDE SEQUENCE. RA Wilson R.K., Warren W., Dotson E., Oliveira P.L.; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EnsemblMetazoa:RPRC000698-PA} RP IDENTIFICATION. RG EnsemblMetazoa; RL Submitted (MAY-2015) to UniProtKB. CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; ACPB03027601; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 13249.RPRC000698-PA; -. DR EnsemblMetazoa; RPRC000698-RA; RPRC000698-PA; RPRC000698. DR VEuPathDB; VectorBase:RPRC000698; -. DR eggNOG; KOG2436; Eukaryota. DR eggNOG; KOG4354; Eukaryota. DR HOGENOM; CLU_034998_0_0_1; -. DR InParanoid; T1H9J5; -. DR OrthoDB; 987250at2759; -. DR Proteomes; UP000015103; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0003991; F:acetylglutamate kinase activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:InterPro. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd04249; AAK_NAGK-NC; 1. DR Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR HAMAP; MF_00082; ArgB; 1. DR InterPro; IPR036393; AceGlu_kinase-like_sf. DR InterPro; IPR004662; AcgluKinase_fam. DR InterPro; IPR023013; AGPR_AS. DR InterPro; IPR037528; ArgB. DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR041731; NAGK-NC. DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd. DR PANTHER; PTHR32338:SF10; N-ACETYL-GAMMA-GLUTAMYL-PHOSPHATE REDUCTASE, CHLOROPLASTIC-RELATED; 1. DR PANTHER; PTHR32338; N-ACETYL-GAMMA-GLUTAMYL-PHOSPHATE REDUCTASE, CHLOROPLASTIC-RELATED-RELATED; 1. DR Pfam; PF00696; AA_kinase; 1. DR Pfam; PF01118; Semialdhyde_dh; 1. DR SMART; SM00859; Semialdhyde_dh; 1. DR SUPFAM; SSF53633; Carbamate kinase-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR TIGRFAMs; TIGR00761; argB; 1. DR PROSITE; PS01224; ARGC; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605}; KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Kinase {ECO:0000256|ARBA:ARBA00022777}; KW NADP {ECO:0000256|ARBA:ARBA00022857}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}; KW Reference proteome {ECO:0000313|Proteomes:UP000015103}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 1..120 FT /note="Semialdehyde dehydrogenase NAD-binding" FT /evidence="ECO:0000259|SMART:SM00859" SQ SEQUENCE 442 AA; 46575 MW; 2D868AEE10FD67F5 CRC64; MNLTALAVSA QSVDAGKRIS DLHPQLKGII DLPVQALTDA AEAAKGIDVV FLATDHKVSH DLAPVFLAAG CVVFDLSGAF RVQDAEFYRR YYGFEHQHAD WLAQAVYGLA EFQAERVKQA QLIAVPGCYP TASQLALKPL VDAQLLNTDL WPVINAVSGV SGAGRKASLT SSFCEVSLQP YGTKAMNPLI IKLGGVLLDS EEALERLFTA LVAYREQYQR PLVIVHGGGC LVDDLMKKLA LPVVKKNGLR VTPADQIDII TGALAGSANK TLLAWAKKHA INAVGLCLVD GGMSTVTQLD ESLGYVGKAQ AGSADLPNAL LSAGYLPIVS SIGITEQGDL MNVNADQAAT ALAETLGADL ILLSDVSGIL DAKGQRIAEM TAQKAEQLIA KGIITDGMIV KVNAALDAAR ALGRPVDIAS WRHADQLPAL FNGTPIGTRI LA //